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?:abstract
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Severe acute respiratory syndrome coronavirus 2(SARS-CoV-2), which causes coronavirus disease (COVID-19), is a novel beta coronavirus. SARS-CoV-2 uses spike glycoprotein to interact with host angiotensin-converting enzyme 2 (ACE2) and ensure cell recognition. High infectivity of SARS-CoV-2 raises questions on spike-ACE2 binding affinity and its neutralization by anti-SARS-CoV monoclonal antibodies (mAbs). Here, we observed Val-to-Lys417 mutation in the receptor-binding domains (RBD) of SARS-CoV-2, which established a Lys-Asp electrostatic interaction enhancing its ACE2-binding. Pro-to-Ala475 substitution and Gly482 insertion in the AGSTPCNGV-loop of RBD possibly hinders neutralization of SARS-CoV-2 by anti-SARS-CoV mAbs. In addition, we identified unique and structurally conserved conformational-epitopes on RBDs, which can be potential therapeutic targets. Collectively, we provide new insights into the mechanisms underlying the high infectivity of SARS-CoV-2 and development of effective neutralizing agents.
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?:doi
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10.1016/j.csbj.2020.11.002
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Comput_Struct_Biotechnol_J
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document_parses/pdf_json/d2abbc5e65b924fc59bcf6e1918dc1193210397c.json
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Mutations in the SARS-CoV-2 Spike RBD are responsible for stronger ACE2 binding and poor anti-SARS-CoV mAbs cross-neutralization
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